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Mol. Cell. Biol., 10 1997, 5823-5832, Vol 17, No. 10
JL Goodier, H Fan and RJ Maraia
Human La protein has been shown to serve as a transcription factor for RNA
polymerase III (pol III) by facilitating transcription termination and
recycling of transcription complexes. In addition, La binds to the 3'
oligo(U) ends common to all nascent pol III transcripts, and in the case of
B1-Alu RNA, protects it from 3'-end processing (R. J. Maraia, D. J. Kenan,
and J. D. Keene, Mol. Cell. Biol. 14:2147-2158, 1994). Others have
previously dissected the La protein into an N-terminal domain that binds
RNA and a C-terminal domain that does not. Here, deletion and substitution
mutants of La were examined for general RNA binding, RNA 3'-end protection,
and transcription factor activity. Although some La mutants altered in a
C-terminal basic region bind RNA in mobility shift assays, they are
defective in RNA 3'-end protection and do not support transcription, while
one C-terminal substitution mutant is defective only in transcription.
Moreover, a C-terminal fragment lacking RNA binding activity appears able
to support low levels of transcription by pol III. While efficient
multiround transcription is supported only by mutants that bind RNA and
contain a C-terminal basic region. These analyses indicate that RNA binding
contributes to but is not sufficient for La transcription factor activity
and that the C-terminal domain plays a role in transcription that is
distinguishable from simple RNA binding. The transcription factor activity
of La can be reversibly inhibited by RNA, suggesting the potential for
feedback inhibition of pol III transcription.
Copyright © 1997, American Society for Microbiology
A carboxy-terminal basic region controls RNA polymerase III transcription factor activity of human La protein
Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.
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